7T7J
Crystal Structure of Phosphoserine aminotransferase from Klebsiella pneumoniae subsp. pneumoniae in complex with Pyridoxal phosphate
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004648 | molecular_function | O-phospho-L-serine:2-oxoglutarate aminotransferase activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006564 | biological_process | L-serine biosynthetic process |
| A | 0008615 | biological_process | pyridoxine biosynthetic process |
| A | 0030170 | molecular_function | pyridoxal phosphate binding |
| B | 0004648 | molecular_function | O-phospho-L-serine:2-oxoglutarate aminotransferase activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0006564 | biological_process | L-serine biosynthetic process |
| B | 0008615 | biological_process | pyridoxine biosynthetic process |
| B | 0030170 | molecular_function | pyridoxal phosphate binding |
Functional Information from PROSITE/UniProt
| site_id | PS00595 |
| Number of Residues | 20 |
| Details | AA_TRANSFER_CLASS_5 Aminotransferases class-V pyridoxal-phosphate attachment site. FGVIyaGAQKnigpa.GlTlV |
| Chain | Residue | Details |
| A | PHE189-VAL208 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 16 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00160","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-(pyridoxal phosphate)lysine","evidences":[{"source":"HAMAP-Rule","id":"MF_00160","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
